메뉴 건너뛰기




Volumn 84, Issue 2 I, 2003, Pages 1238-1251

Effects of water soluble phosphotidylserine on bovine factor Xa: Functional and structural changes plus dimerization

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10A; PHOSPHATIDYLSERINE; PHOSPHOLIPID;

EID: 0037306106     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74939-X     Document Type: Article
Times cited : (21)

References (49)
  • 5
    • 0017342164 scopus 로고
    • Molecular weights of protein multimers from polyacrylamide gel electrophoresis
    • Bryan, J. K. 1977. Molecular weights of protein multimers from polyacrylamide gel electrophoresis. Anal Biochem. 78:513-519.
    • (1977) Anal. Biochem. , vol.78 , pp. 513-519
    • Bryan, J.K.1
  • 6
    • 0030890565 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer study of shape changes in membrane-bound bovine prothrombin and meizothrombin
    • Chen, Q., and B. R. Lentz. 1997. Fluorescence resonance energy transfer study of shape changes in membrane-bound bovine prothrombin and meizothrombin. Biochemistry. 36:4701-4711.
    • (1997) Biochemistry , vol.36 , pp. 4701-4711
    • Chen, Q.1    Lentz, B.R.2
  • 7
    • 0029148317 scopus 로고
    • Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid vesicles
    • Christiansen, W. T., L. R. Jalbert, R. M. Robertson, A. Jhingan, M. Prorok, and F. J. Castellino. 1995. Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid vesicles. Biochemistry. 34:10376-10382.
    • (1995) Biochemistry , vol.34 , pp. 10376-10382
    • Christiansen, W.T.1    Jalbert, L.R.2    Robertson, R.M.3    Jhingan, A.4    Prorok, M.5    Castellino, F.J.6
  • 8
    • 0027978049 scopus 로고
    • Assembly of the prothrombinase complex on lipid vesicles depends on the stereochemical configuration of the polar headgroup of phosphatidylserine
    • Comfurius, P., E. F. Smeets, G. M. Willems, E. M. Bevers, and R. F. Zwaal. 1994. Assembly of the prothrombinase complex on lipid vesicles depends on the stereochemical configuration of the polar headgroup of phosphatidylserine. Biochemistry, 33:10319-10324.
    • (1994) Biochemistry , vol.33 , pp. 10319-10324
    • Comfurius, P.1    Smeets, E.F.2    Willems, G.M.3    Bevers, E.M.4    Zwaal, R.F.5
  • 9
    • 0024448191 scopus 로고
    • A new model to describe extrinsic protein binding to phospholipid membranes of varying composition: Application to human coagulation proteins
    • Cutsforth, G. A., R. N. Whitaker, J. Hermans, and B. R. Lentz. 1989. A new model to describe extrinsic protein binding to phospholipid membranes of varying composition: application to human coagulation proteins. Biochemistry. 28:7453-7461.
    • (1989) Biochemistry , vol.28 , pp. 7453-7461
    • Cutsforth, G.A.1    Whitaker, R.N.2    Hermans, J.3    Lentz, B.R.4
  • 10
    • 0035968172 scopus 로고    scopus 로고
    • The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes
    • Falls, L. A., B. C. Furie, M. Jacobs, B. Furie, and A. C. Rigby. 2001. The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes. J. Biol. Chem. 276:23895-23902.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23895-23902
    • Falls, L.A.1    Furie, B.C.2    Jacobs, M.3    Furie, B.4    Rigby, A.C.5
  • 11
    • 0001522673 scopus 로고
    • Ferguson plot analysis
    • Ferguson, K. A. 1964. Ferguson plot analysis. Metabolism. 13:985-1002.
    • (1964) Metabolism , vol.13 , pp. 985-1002
    • Ferguson, K.A.1
  • 12
    • 0016353124 scopus 로고
    • The mechanism of activation of bovine factor X (Stuart factor) by intrinsic and extrinsic pathways
    • Fujikawa, K., M. H. Coan, M. E. Legaz, and E. W. Davie. 1974. The mechanism of activation of bovine factor X (Stuart factor) by intrinsic and extrinsic pathways. Biochemistry. 13:5290-5299.
    • (1974) Biochemistry , vol.13 , pp. 5290-5299
    • Fujikawa, K.1    Coan, M.H.2    Legaz, M.E.3    Davie, E.W.4
  • 13
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and G. D. Fasman. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 14
    • 0016774953 scopus 로고
    • Cooperative calcium binding by the phospholipid binding region of bovine prothrombin: A requirement for intact disulfide bridges
    • Henriksen, R. A., and C. M. Jackson. 1975. Cooperative calcium binding by the phospholipid binding region of bovine prothrombin: a requirement for intact disulfide bridges. Arch. Biochem. Biophys. 170:149-159.
    • (1975) Arch. Biochem. Biophys. , vol.170 , pp. 149-159
    • Henriksen, R.A.1    Jackson, C.M.2
  • 15
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure - Characterization of size distribution, trapped volume and ability to maintain a membrane-potential
    • Hope, M. J., M. B. Bally, G. Webb, and P. R. Cullis. 1985. Production of large unilamellar vesicles by a rapid extrusion procedure - characterization of size distribution, trapped volume and ability to maintain a membrane-potential. Biochim. Biophys. Acta. 812:55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 16
    • 0023518606 scopus 로고
    • a. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex
    • a. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex. J. Biol. Chem. 262:12953-12961.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12953-12961
    • Husten, E.J.1    Esmon, C.T.2    Johnson, A.E.3
  • 19
    • 0017246524 scopus 로고
    • The activation of bovine coagulation factor X
    • Jesty, J., and Y. Nemerson. 1976. The activation of bovine coagulation factor X. Methods Enzyme 45:95-107.
    • (1976) Methods Enzyme , vol.45 , pp. 95-107
    • Jesty, J.1    Nemerson, Y.2
  • 20
    • 0016706604 scopus 로고
    • The activation of coagulation factor X. Identity of cleavage sites in the alternative activation pathways and characterization of the COOH-terminal peptide
    • Jesty, J., A. K. Spencer, Y. Nakashima, Y. Nemerson, and W. Konigsberg. 1975. The activation of coagulation factor X. Identity of cleavage sites in the alternative activation pathways and characterization of the COOH-terminal peptide. J. Biol. Chem. 250:4497-4504.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4497-4504
    • Jesty, J.1    Spencer, A.K.2    Nakashima, Y.3    Nemerson, Y.4    Konigsberg, W.5
  • 21
    • 0016294181 scopus 로고
    • The mechanism of activation of factor X. Kinetic control of alternative pathways leading to the formation of activated factor X
    • Jesty, J., A. K. Spencer, and Y. Nemerson. 1974. The mechanism of activation of factor X. Kinetic control of alternative pathways leading to the formation of activated factor X. J. Biol. Chem. 249: 5614-5622.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5614-5622
    • Jesty, J.1    Spencer, A.K.2    Nemerson, Y.3
  • 22
    • 0019451876 scopus 로고
    • Thermodynamics of dihexanoylphosphatidylcholine aggregation
    • Johnson, R. E., M. A. Wells, and J. A. Rupley. 1981. Thermodynamics of dihexanoylphosphatidylcholine aggregation. Biochemistry. 20:4239-4242.
    • (1981) Biochemistry , vol.20 , pp. 4239-4242
    • Johnson, R.E.1    Wells, M.A.2    Rupley, J.A.3
  • 23
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C., Jr. 1990. Protein secondary structure and circular dichroism: a practical guide. Proteins. 7:205-214.
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson W.C., Jr.1
  • 24
    • 0022381687 scopus 로고
    • Comparison of the abilities of synthetic and platelet-derived membranes to enhance thrombin formation
    • Jones, M. E., B. R. Lentz, F. A. Dombrose, and H. Sandberg. 1985. Comparison of the abilities of synthetic and platelet-derived membranes to enhance thrombin formation. Thromb. Res. 39:711-724.
    • (1985) Thromb. Res. , vol.39 , pp. 711-724
    • Jones, M.E.1    Lentz, B.R.2    Dombrose, F.A.3    Sandberg, H.4
  • 26
    • 0016861462 scopus 로고
    • Protein interactions with small molecules. Relationships between stoichiometric binding constants, site binding constants, and empirical binding parameters
    • Klotz, I. M., and D. L. Hunston. 1975. Protein interactions with small molecules. Relationships between stoichiometric binding constants, site binding constants, and empirical binding parameters. J. Biol. Chem. 250:3001-3009.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3001-3009
    • Klotz, I.M.1    Hunston, D.L.2
  • 28
    • 0017745217 scopus 로고
    • Structure of the prothrombin- and blood clotting factor X-membrane complexes
    • Lim, T. K., V. A. Bloomfield, and G. L. Nelsestuen. 1977. Structure of the prothrombin- and blood clotting factor X-membrane complexes. Biochemistry. 16:4177-4181.
    • (1977) Biochemistry , vol.16 , pp. 4177-4181
    • Lim, T.K.1    Bloomfield, V.A.2    Nelsestuen, G.L.3
  • 29
    • 0037119399 scopus 로고    scopus 로고
    • Soluble phosphatidylserine triggers assembly in solution of a prothrombin-activating complex in the absence of a membrane surface
    • In press
    • Majumder, R., G. Weinreb, X. Zhai, and B. R. Lentz. 2002. Soluble phosphatidylserine triggers assembly in solution of a prothrombin-activating complex in the absence of a membrane surface. J. Biol. Chem. In press.
    • (2002) J. Biol. Chem.
    • Majumder, R.1    Weinreb, G.2    Zhai, X.3    Lentz, B.R.4
  • 30
    • 0017275076 scopus 로고
    • Prothrombin
    • Mann, K. G. 1976. Prothrombin. Methods Enzymol. 45:123-156.
    • (1976) Methods Enzymol. , vol.45 , pp. 123-156
    • Mann, K.G.1
  • 31
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann, K. G., M. E. Nesheim, W. R. Church, P. Haley, and S. Krishnaswamy. 1990. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood. 76:1-16.
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 32
    • 0030967015 scopus 로고    scopus 로고
    • Comparison of naturally occurring vitamin K-dependent proteins: Correlation of amino acid sequences and membrane binding properties suggests a membrane contact site
    • McDonald, J. F., A. M. Shah, R. A. Schwalbe, W. Kisiel, B. Dahlback, and G. L. Nelsestuen. 1997. Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site. Biochemistry. 36:5120-5127.
    • (1997) Biochemistry , vol.36 , pp. 5120-5127
    • McDonald, J.F.1    Shah, A.M.2    Schwalbe, R.A.3    Kisiel, W.4    Dahlback, B.5    Nelsestuen, G.L.6
  • 33
    • 0028172974 scopus 로고
    • A staining procedure using Coomassie brilliant blue G-250 in phosphoric acid for detection of protein bands with high resolution in polyacrylamide gel and nitrocellulose membrane
    • Mitra, P., A. K. Pal, D. Basu, and R. N. Hati. 1994. A staining procedure using Coomassie brilliant blue G-250 in phosphoric acid for detection of protein bands with high resolution in polyacrylamide gel and nitrocellulose membrane. Anal. Biochem. 223:327-329.
    • (1994) Anal. Biochem. , vol.223 , pp. 327-329
    • Mitra, P.1    Pal, A.K.2    Basu, D.3    Hati, R.N.4
  • 35
    • 0027425514 scopus 로고
    • Comparison of the membrane binding kinetics of bovine prothrombin and its fragment I
    • Pearce, K. H., M. Hof, B. R. Lentz, and N. L. Thompson. 1993. Comparison of the membrane binding kinetics of bovine prothrombin and its fragment I. J. Biol. Chem. 268:22984-22991.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22984-22991
    • Pearce, K.H.1    Hof, M.2    Lentz, B.R.3    Thompson, N.L.4
  • 37
    • 0034701009 scopus 로고    scopus 로고
    • a: Role of sodium in the prothrombinase complex
    • a: role of sodium in the prothrombinase complex. Biochemistry. 39: 1817-1825.
    • (2000) Biochemistry , vol.39 , pp. 1817-1825
    • Rezaie, A.R.1    He, X.2
  • 38
    • 0023869983 scopus 로고
    • Prothrombin activation on phospholipid membranes with positive electrostatic potential
    • Rosing, J., H. Speijer, and R. F. Zwaal. 1988. Prothrombin activation on phospholipid membranes with positive electrostatic potential. Biochemistry. 27:8-11.
    • (1988) Biochemistry , vol.27 , pp. 8-11
    • Rosing, J.1    Speijer, H.2    Zwaal, R.F.3
  • 40
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N., and R. W. Woody. 2000. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287:252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 42
    • 0025316949 scopus 로고
    • Evaluation of membrane phase behavior as a tool to detect extrinsic protein-induced domain formation: Binding of prothrombin to phosphatidylserine/phosphatidylcholine vesicles
    • Tendian, S. W., and B. R. Lentz. 1990. Evaluation of membrane phase behavior as a tool to detect extrinsic protein-induced domain formation: binding of prothrombin to phosphatidylserine/phosphatidylcholine vesicles. Biochemistry. 29:6720-6729.
    • (1990) Biochemistry , vol.29 , pp. 6720-6729
    • Tendian, S.W.1    Lentz, B.R.2
  • 43
    • 0002312258 scopus 로고
    • A model for assembly of coagulation factor complexes on cell surfaces: Prothrombin activation on platelets
    • D. Phillips and M. Shuman, editors. Academic Press, Toronto
    • Tracy, P., and K. Mann. 1986. A model for assembly of coagulation factor complexes on cell surfaces: Prothrombin activation on platelets. In Biochemistry of Platelet. D. Phillips and M. Shuman, editors. Academic Press, Toronto. 295-318.
    • (1986) Biochemistry of Platelet , pp. 295-318
    • Tracy, P.1    Mann, K.2
  • 44
    • 0023805430 scopus 로고
    • Regulation of thrombin generation at cell surfaces
    • Tracy, P. B. 1988. Regulation of thrombin generation at cell surfaces. Semin. Thromb. Hemost. 14:227-233.
    • (1988) Semin. Thromb. Hemost. , vol.14 , pp. 227-233
    • Tracy, P.B.1
  • 45
    • 0021915583 scopus 로고
    • Human prothrombinase complex assembly and function on isolated peripheral blood cell populations
    • Tracy, P. B., L. L. Eide, and K. G. Mann. 1985. Human prothrombinase complex assembly and function on isolated peripheral blood cell populations. J. Biol. Chem. 260:2119-2124.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2119-2124
    • Tracy, P.B.1    Eide, L.L.2    Mann, K.G.3
  • 47
    • 0019777004 scopus 로고
    • Simple and rapid method to determine the binding of blood clotting factor X to phospholipid vesicles
    • van Dieijen, G., G. Tans, J. van Rijn, R. F. Zwaal, and J. Rosing, 1981. Simple and rapid method to determine the binding of blood clotting factor X to phospholipid vesicles. Biochemistry. 20: 7096-7101.
    • (1981) Biochemistry , vol.20 , pp. 7096-7101
    • Van Dieijen, G.1    Tans, G.2    Van Rijn, J.3    Zwaal, R.F.4    Rosing, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.